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Title 

Molecular properties of global suppressors of temperature-sensitive folding mutations in P22 tailspike endorhamnosidase

Authors 

Sang Chul LeeHeyeong KohMyeong Hee Yu

Publisher 

American Society for Biochemistry and Molecular Biology

Issue Date 

1991

Citation 

Journal of Biological Chemistry, vol. 266, no. 34, pp. 23191-23196

Keywords 

suppressor factorbacteriophage p22protein foldingtemperature sensitivityvirus mutationtemperature

Abstract 

Two global suppressors (Val-331 > Ala and Ala-334 > Val) have been identified for temperature-sensitive folding (tsf) mutations in gene 9 of bacteriophage P22 (Mitraki, A., Fane, B., Haase-Pettingell, C., Sturtevant, J., and King, J. (1991) Science 253, 54-58). We have introduced 19 different single amino acid substitutions at the two global suppressor sites independently and examined the effects on the tailspike formation in Escherichia coli. Folding and maturation patterns of the various substitutions at the two global suppressor sites in the wild-type background suggest that Val-331 is located on the protein surface and Ala-334 is in the hydrophobic region. In combination with a tsf mutation, tsfH304 (Gly-244 > Arg), only Gly at 331 and Ile at 334, the substitutions that have similar side chain properties to the original suppressor sequences, were active as tsf suppressors. The newly identified suppressors of tsfH304 could also alleviate the tsf defect of three other mutations. The mutant carrying both Val-331 > Ala and Ala-334 > Val substitutions was also a global suppressor and was more active in suppressing the tsf defect than mutants carrying only one substitution. The suppressors may act by increasing the stability of an intermediate in the productive pathway of folding and maturation of the mutant polypeptides.

ISSN 

0021-9258

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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